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10.1080/15548627.2015.1091141 http://scihub22266oqcxt.onion/10.1080/15548627.2015.1091141 C4824587!4824587!26389781     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Autophagy 2015 ; 11 (11): 1956-77 Nephropedia Template TP {{tp|p=26389781|t=2015. ER stress: Autophagy induction, inhibition and selection |pdf=|usr=}}{{26389781}} gab.com Text ER stress: Autophagy induction, inhibition and selection JO: Autophagy http://www.kidney.de/pget.php?&tw=1&pmid=26389781 #FOAvip An accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER) leads to stress conditions. To mitigate such circumstances, stressed cells activate a homeostatic intracellular signaling network cumulatively called the unfolded protein response (UPR), which orchestrates the recuperation of ER function. Macroautophagy (hereafter autophagy), an intracellular lysosome-mediated bulk degradation pathway for recycling and eliminating wornout proteins, protein aggregates, and damaged organelles, has also emerged as an essential protective mechanism during ER stress. These 2 systems are dynamically interconnected, and recent investigations have revealed that ER stress can either stimulate or inhibit autophagy. However, the stress-associated molecular cues that control the changeover switch between induction and inhibition of autophagy are largely obscure. This review summarizes the crosstalk between ER stress and autophagy and their signaling networks mainly in mammalian-based systems. Additionally, we highlight current knowledge on selective autophagy and its connection to ER stress. Twit Text FOAVip ER stress: Autophagy induction, inhibition and selection ????Autophagy http://www.kidney.de/pget.php?&tw=1&pmid=26389781 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26389781 #FOAvip English Wikipedia <ref>{{Cite pmid|26389781}}</ref> ER stress: Autophagy induction, inhibition and selection #MMPMID26389781 Rashid HO; Yadav RK; Kim HR; Chae HJ Autophagy 2015[Nov]; 11 (11): 1956-77 PMID26389781show ga An accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER) leads to stress conditions. To mitigate such circumstances, stressed cells activate a homeostatic intracellular signaling network cumulatively called the unfolded protein response (UPR), which orchestrates the recuperation of ER function. Macroautophagy (hereafter autophagy), an intracellular lysosome-mediated bulk degradation pathway for recycling and eliminating wornout proteins, protein aggregates, and damaged organelles, has also emerged as an essential protective mechanism during ER stress. These 2 systems are dynamically interconnected, and recent investigations have revealed that ER stress can either stimulate or inhibit autophagy. However, the stress-associated molecular cues that control the changeover switch between induction and inhibition of autophagy are largely obscure. This review summarizes the crosstalk between ER stress and autophagy and their signaling networks mainly in mammalian-based systems. Additionally, we highlight current knowledge on selective autophagy and its connection to ER stress. äER stress: Autophagy induction, inhibition and selection (epmc).pdf DeepDyve Pubget Overpricing